Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 21, Issue 13, Pages 4089-4096Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/MCB.21.13.4089-4096.2001
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Funding
- NIGMS NIH HHS [R01 GM052486, R01 GM060479, GM52486, GM60479] Funding Source: Medline
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BUR1, which was previously identified by a selection for mutations that have general effects on transcription in Saccharomyces cerevisiae, encodes a cyclin-dependent kinase that is essential for viability, but none of its substrates have been identified to date. Using an unbiased biochemical approach, we have identified the carboxy-terminal domain (CTD) of Rpb1, the largest subunit of RNA polymerase II, as a Bur1 substrate. Phosphorylation of Rpb1 by Bur1 is likely to be physiologically relevant, since burl mutations interact genetically with rpb1 CTD truncations and with mutations in other genes involved in CTD function. Several genetic interactions are presented, implying a role for Burl during transcriptional elongation. These results identify Burl as a fourth S. cerevisiae CTD kinase and provide striking functional similarities between Bur1 and metazoan P-TEFb.
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